Human cytomegalovirus is an enveloped, double-stranded DNA virus of the family. Herpesviridae with estimates of seropositivity ranging from 45 to 100% in different populations around the world. Human cytomegalovirus (HCMV) encodes multiple surface glycoprotein complexes to infect a variety of cell types. Infection amongst adults is frequent and infected individuals rarely experience symptoms. The virus lies dormant in the body after infection. The trouble arises with immunocompromised individuals such as transplant patients and pregnant women as it is possible to cause birth defects in infants. Despite the severity of these infections and the prevalence of this pathogen, there are currently no U.S. Food and Drug Administration–approved vaccines and therapeutic options remain limited. The Three main responsible glycol proteins are gB, the trimer made from gH/gL/GO, and the pentamer made from gH/gL/UL28/UL130/UL131A. The pentamer helps the virus enter epithelial and endothelial cells and is one of the targets for antibody therapeutics. Recently a paper by (Wrapp D., et al) from the McLellan lab characterized the structure of pentamer to its binding site NRP2 and fabs 1-103 and 1-32 which neutralize HCMV, through Cryo-EM. The purpose of my project is to computationally come as close as possible to determining the position of the two antibodies used compared to the cryo em structure that has been published.